What is it about?
In this study, we report the molecular, biochemical, and structural characterization of ADC-68, which is a class C extended-spectrum β-lactamase (cESBL) and carbapenemase, from A. baumannii D015.
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Why is it important?
ADC-68 is the first reported enzyme among chromosomal class C β-lactamases to possess class C extended-spectrum β-lactamase and carbapenemase activities.
Perspectives
Based on the multidrug-resistant characteristics of ADC-68, which is resistant to carbapenems as well as extended-spectrum cephalosporins, drugs for the treatment of an ADC-68-producing pathogen can be developed using an extended-spectrum mechanism that considers the following points: (a) the pathogen was resistant to carbapenems as well as extended-spectrum cephalosporins; (b) three clinically used inhibitors had little (or no) effect on ADC-68 that had cESBL and carbapenemase activity; and (c) if an IS element (such as ISAba1) is inserted before the direct repeat sequence of blaADC-68, ADC-68 could be more resistant to these β-lactams.
Professor Sang Hee Lee
Myongji University
Read the Original
This page is a summary of: Structure of ADC-68, a novel carbapenem-hydrolyzing class C extended-spectrum β-lactamase isolated fromAcinetobacter baumannii, Acta Crystallographica Section D Biological Crystallography, October 2014, International Union of Crystallography,
DOI: 10.1107/s1399004714019543.
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